2E3X

Crystal structure of Russell's viper venom metalloproteinase

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2e3xb_	Alpha and beta proteins (a+b)	C-type lectin-like	C-type lectin-like	automated matches	automated matches	(Daboia siamensis ) [TaxId: 343250 ],	SCOPe (2.08)
C	d2e3xc_	Alpha and beta proteins (a+b)	C-type lectin-like	C-type lectin-like	automated matches	automated matches	(Daboia siamensis ) [TaxId: 343250 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2 Family	C-type lectin domain	8065485	4002453	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	C-type lectin-like	8065486	3001261	SCOP2 (2022-06-29)
C	SCOP2 Family	C-type lectin domain	8065499	4002453	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	C-type lectin-like	8065500	3001261	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF01421	e2e3xA1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01421	ECOD (1.6)
A	PF08516	e2e3xA3	A: few secondary structure elements	X: Disulfide-rich domain in A Disintegrin And Metalloprotease (ADAM) domain-containing proteins (From Topology)	H: Disulfide-rich domain in A Disintegrin And Metalloprotease (ADAM) domain-containing proteins (From Topology)	T: Disulfide-rich domain in A Disintegrin And Metalloprotease (ADAM) domain-containing proteins	F: PF08516	ECOD (1.6)
A	PF00200	e2e3xA2	A: few secondary structure elements	X: Blood coagulation inhibitor (disintegrin) (From Topology)	H: Blood coagulation inhibitor (disintegrin) (From Topology)	T: Blood coagulation inhibitor (disintegrin)	F: PF00200	ECOD (1.6)
B	PF00059	e2e3xB1	A: a+b complex topology	X: C-type lectin-like (From Homology)	H: C-type lectin-like	T: C-type lectin-like	F: PF00059	ECOD (1.6)
C	PF00059	e2e3xC1	A: a+b complex topology	X: C-type lectin-like (From Homology)	H: C-type lectin-like	T: C-type lectin-like	F: PF00059	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
B	3.10.100.10	Alpha Beta	Roll	Mannose-Binding Protein A	Chain A	CATH (4.3.0)
C	3.10.100.10	Alpha Beta	Roll	Mannose-Binding Protein A	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF08516	ADAM cysteine-rich (ADAM_CR)	ADAM cysteine-rich	-	Family
A	PF00200	Disintegrin (Disintegrin)	Disintegrin	-	Domain
A	PF01421	Reprolysin (M12B) family zinc metalloprotease (Reprolysin)	Reprolysin (M12B) family zinc metalloprotease	The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammal ...	The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin Swiss:Q28472. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.	Domain
B	PF00059	Lectin C-type domain (Lectin_C)	Lectin C-type domain	This family includes both long and short form C-type	Domain
C	PF00059	Lectin C-type domain (Lectin_C)	Lectin C-type domain	This family includes both long and short form C-type	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Coagulation factor X-activating enzyme heavy chain	peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase activity catalytic activity endopeptidase activity toxin activity cation binding ion binding binding metal ion binding small molecule binding	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	extracellular region cellular anatomical entity
B	Coagulation factor X-activating enzyme light chain 2	cation binding ion binding binding metal ion binding small molecule binding toxin activity	-	extracellular region cellular anatomical entity
C	Coagulation factor X-activating enzyme light chain 1	cation binding ion binding binding metal ion binding small molecule binding toxin activity	-	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR034027	Reprolysin domain, adamalysin-type	Domain
A	IPR024079	Metallopeptidase, catalytic domain superfamily	Homologous Superfamily
A	IPR018358	Disintegrin, conserved site	Conserved Site
A	IPR001762	Disintegrin domain	Domain
A	IPR002870	Peptidase M12B, propeptide	Domain
A	IPR001590	Peptidase M12B, ADAM/reprolysin	Domain
A	IPR006586	ADAM, cysteine-rich domain	Domain
A	IPR036436	Disintegrin domain superfamily	Homologous Superfamily
B	IPR001304	C-type lectin-like	Domain
B	IPR018378	C-type lectin, conserved site	Conserved Site
B	IPR016186	C-type lectin-like/link domain superfamily	Homologous Superfamily
B	IPR016187	C-type lectin fold	Homologous Superfamily
C	IPR001304	C-type lectin-like	Domain
C	IPR018378	C-type lectin, conserved site	Conserved Site
C	IPR016186	C-type lectin-like/link domain superfamily	Homologous Superfamily
C	IPR016187	C-type lectin fold	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.